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5KC9

Crystal structure of the amino-terminal domain (ATD) of iGluR Delta-1 (GluD1)

Summary for 5KC9
Entry DOI10.2210/pdb5kc9/pdb
DescriptorGlutamate receptor ionotropic, delta-1, 1,2-ETHANEDIOL, CHLORIDE ION, ... (7 entities in total)
Functional Keywordsionotropic glutamate receptor (iglur), neurotransmission, signaling protein
Biological sourceMus musculus (House mouse)
Total number of polymer chains3
Total formula weight148521.76
Authors
Elegheert, J.,Clay, J.E.,Siebold, C.,Aricescu, A.R. (deposition date: 2016-06-05, release date: 2016-07-27, Last modification date: 2024-10-23)
Primary citationElegheert, J.,Kakegawa, W.,Clay, J.E.,Shanks, N.F.,Behiels, E.,Matsuda, K.,Kohda, K.,Miura, E.,Rossmann, M.,Mitakidis, N.,Motohashi, J.,Chang, V.T.,Siebold, C.,Greger, I.H.,Nakagawa, T.,Yuzaki, M.,Aricescu, A.R.
Structural basis for integration of GluD receptors within synaptic organizer complexes.
Science, 353:295-299, 2016
Cited by
PubMed Abstract: Ionotropic glutamate receptor (iGluR) family members are integrated into supramolecular complexes that modulate their location and function at excitatory synapses. However, a lack of structural information beyond isolated receptors or fragments thereof currently limits the mechanistic understanding of physiological iGluR signaling. Here, we report structural and functional analyses of the prototypical molecular bridge linking postsynaptic iGluR δ2 (GluD2) and presynaptic β-neurexin 1 (β-NRX1) via Cbln1, a C1q-like synaptic organizer. We show how Cbln1 hexamers "anchor" GluD2 amino-terminal domain dimers to monomeric β-NRX1. This arrangement promotes synaptogenesis and is essential for D: -serine-dependent GluD2 signaling in vivo, which underlies long-term depression of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses and motor coordination in developing mice. These results lead to a model where protein and small-molecule ligands synergistically control synaptic iGluR function.
PubMed: 27418511
DOI: 10.1126/science.aae0104
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

238268

數據於2025-07-02公開中

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